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- W3025891904 endingPage "51" @default.
- W3025891904 startingPage "1" @default.
- W3025891904 abstract "The past decade has witnessed a significant growth in the identification of allosteric modulators of G protein–coupled receptors (GPCRs), i.e., ligands that interact with binding sites that are topographically distinct from the orthosteric site recognized by the receptor's endogenous agonist. Because of their ability to modulate receptor conformations in the presence of orthosteric ligand, allosteric modulators can “fine-tune” classical pharmacological responses. This is advantageous in terms of a potential for engendering greater GPCR subtype-selectivity, but represents a significant challenge for detecting and validating allosteric behaviors. Although allosteric sites need not have evolved to accommodate endogenous ligands, there are a number of examples of where such modulators have been shown to contribute to physiological or pathophysiological processes. Studies are also beginning to unravel the structural basis of allosteric modulation of GPCRs. It remains to be determined whether such modulation represents interactions within monomers versus across dimers." @default.
- W3025891904 created "2020-05-21" @default.
- W3025891904 creator A5016689951 @default.
- W3025891904 creator A5075216835 @default.
- W3025891904 creator A5075463548 @default.
- W3025891904 creator A5077280255 @default.
- W3025891904 date "2007-02-01" @default.
- W3025891904 modified "2023-10-18" @default.
- W3025891904 title "Allosteric Modulation of G Protein–Coupled Receptors" @default.
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